Figure 2: MKP7-CD is crucial for JNK1 binding and enzyme catalysis. | Nature Communications

Figure 2: MKP7-CD is crucial for JNK1 binding and enzyme catalysis.

From: A conserved motif in JNK/p38-specific MAPK phosphatases as a determinant for JNK1 recognition and inactivation

Figure 2

(a) Domain organization of human MKP7 and JNK1. The KBD and CD of MKP7 are shown in green and blue, and the N-lobe and C-lobe of JNK1 are coloured in lemon and yellow, respectively. The key structural elements are indicated. The colour scheme is the same in the following figures unless indicated otherwise. (b) Plots of initial velocity of the MKP7-catalysed reaction versus phospho-JNK1 concentration. The solid lines are best-fitting results according to equation (1). Each experiment was performed in replicate for at least three times. The error bars represent s.e.m. (c) Gel filtration analysis for interaction of JNK1 with MKP7-CD and MKP7-KBD. (d) GST-mediated pull-down assay for interaction of JNK1 with MKP7-CD and MKP7-KBD. The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays. The protein amounts of MKP7 used are shown at the bottom.

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